1b4w: Difference between revisions

Revision as of 18:16, 30 June 2008

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File:1b4w.png

Template:STRUCTURE 1b4w

BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHYBASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY

Template:ABSTRACT PUBMED 10728829

About this StructureAbout this Structure

1B4W is a Single protein structure of sequence from Gloydius halys. Full crystallographic information is available from OCA.

ReferenceReference

Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities., Zhao K, Zhou Y, Lin Z, Toxicon. 2000 Jul;38(7):901-16. PMID:10728829

Page seeded by OCA on Mon Jun 30 18:16:10 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1b4w.gif|left|200px]]
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 {{STRUCTURE_1b4w|  PDB=1b4w  |  SCENE=  }}
-'''BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY'''
+===BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY===
-==Overview==
+<!--
-The basic phospholipase A2 (PLA2) from the venom of Agkistrodon halys Pallas is a potent hemolytic toxin and anticoagulant. Crystal structure of the enzyme complexed with detergent n-octyl beta-D-glucopyranoside (beta-OG) in monoclinic crystal form has been determined to 2.6 A resolution. Beta-OG molecules were found in the hydrophobic channels of the enzyme. SDS-PAGE and dynamic light scattering measurements showed that the enzyme had a strong tendency to dimerise in aqueous solution. In the crystal structure the enzyme molecules associate into a tetramer with pseudo 222 symmetry, and the interfacial recognition site linked dimers constituting the tetramer have intensive interface interactions, and may be stable in solution. The structure reveals a unique positively charged face at the C-terminal region and a characteristic non-cationic 'anticoagulant' region (53-77). The face is supposed to be the hemolytic site, and based on sequence and structure comparison residues Trp70 and Glu53 instead of the basic residues in 'anticoagulant' region might play an important role in the anticoagulant activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_10728829}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10728829 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10728829}}
 ==About this Structure==
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 [[Category: Basic phospholipase a2]]
 [[Category: Dimer]]
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